The Enzyme Database

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EC 3.5.3.1     
Accepted name: arginase
Reaction: L-arginine + H2O = L-ornithine + urea
For diagram of the urea cycle and arginine biosynthesis, click here
Other name(s): arginine amidinase; canavanase; L-arginase; arginine transamidinase
Systematic name: L-arginine amidinohydrolase
Comments: Also hydrolyses α-N-substituted L-arginines and canavanine.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9000-96-8
References:
1.  Bach, S.J. and Killip, J.D. Studies on the purification and the kinetic properties of arginase from beef, sheep and horse liver. Biochim. Biophys. Acta 47 (1961) 336–343. [PMID: 13685626]
2.  Cabello, J., Basilio, C. and Prajoux, V. Kinetic properties of erythrocyte- and liver arginase. Biochim. Biophys. Acta 48 (1961) 148–152. [PMID: 13689647]
3.  Dumitru, I.F. Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight. Acta Vitamin. Enzymol. 27 (1973) 207–210. [PMID: 4801830]
4.  Greenberg, D.M. Arginase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 257–267.
5.  Greenberg, D.M., Bagot, A.E. and Roholt, O.A. Liver arginase. III. Properties of highly purified arginase. Arch. Biochem. Biophys. 62 (1956) 446–453. [PMID: 13328133]
[EC 3.5.3.1 created 1961]
 
 


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